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兔血浆α_2-巨球蛋白的分离纯化
引用本文:鲍玉洲,杨丙辛,张春艳. 兔血浆α_2-巨球蛋白的分离纯化[J]. 河南医学研究, 1996, 0(1)
作者姓名:鲍玉洲  杨丙辛  张春艳
作者单位:河南省眼科研究所生化室,河南省红十字血液中心,中山医科大学免疫教研室
摘    要:本研究从家兔血浆中分离纯化了α_2-巨球蛋白。首先用利凡诺法从血浆中提取出α_2巨球蛋白粗制品,然后上SephacrylS_(400)凝胶柱过滤后,用琼脂糖凝胶电泳即可得到电泳纯的。α_2巨球蛋白。结合胰蛋白酶活力测定结果表明,α_2-巨球蛋白活性峰与SephacrylS_(400)凝胶过滤的第一洗脱峰完全重合;SDS-聚丙烯酰胺凝胶电泳结果显示出一条单一条带;家兔α_2-巨球蛋白的亚基分子量经测定为178.94KD,与人的α_2-巨球蛋白亚基分子量180KD基本相同。说明用这种方法提取纯化α_2-巨球蛋白是一种切实可行的方法。

关 键 词:α_2-巨球蛋白,家兔,提取纯化

STUDY ON THE ISOLATION AND PURIFICATION OF α_2-MACROGLOBULIN BY RABBIT PLASMA
Bao Yu-zhou ,Yang Bing-xin ,Zhang Chun-yan. STUDY ON THE ISOLATION AND PURIFICATION OF α_2-MACROGLOBULIN BY RABBIT PLASMA[J]. Henan Medical Research, 1996, 0(1)
Authors:Bao Yu-zhou   Yang Bing-xin   Zhang Chun-yan
Abstract:α_2Macroglobulin was successfully isolated and purified by rabbit plasma.α2-Macroglobulin semifinished product was isolated and extracted from rabbit plasma by therivanol method;the semifinished product was first filtrated by Sephacryl S_400 gel,and then thesample was passed through the electrophoretic purified α_2-macroglobulin was obtained. Theactivity determination combined with trypsin showed that the activity peak of α_2-macroglobu-lin and the first peak of the filtration by Sephacryl S_400 were completely coincided. The tesultin the electrophoresis of Sephacryl S_400 gel showed a single zone. The determination to themolecular weight of α_2-macroglobulin suhunit indicated that the molecular weight ofα_2-macroglobulin subunit in rabbit (178.94 KD) is similar to that in human being (180 KD).
Keywords:α_2-macroglobulin  rabbit  extracting  purification
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